› 4kcv

X-ray diffraction
2.18Å resolution

Pyruvate kinase (PYK) from Trypanosoma brucei soaked with 2-oxoglutaric acid

Released:
DOI: 10.2210/pdb4kcv/pdb
PDB entry 4kcv coloured by chain, front view.
PDB entry 4kcv coloured by chain, side view.
PDB entry 4kcv coloured by chain, top view.
Source organism: Trypanosoma brucei brucei
Primary publication:
Pyruvate kinases have an intrinsic and conserved decarboxylase activity.
Zhong W, Morgan HP, Nowicki MW, McNae IW, Yuan M, Bella J, Michels PA, Fothergill-Gilmore LA, Walkinshaw MD
Biochem J 458 301-11 (2014)
PMID: 24328825

Function and Biology Details

Reaction catalysed: 
ATP + pyruvate = ADP + phosphoenolpyruvate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151771 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyruvate kinase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 499 amino acids
Theoretical weight: 54.54 KDa
Source organism: Trypanosoma brucei brucei
Expression system: Escherichia coli
UniProt:
  • Canonical: P30615 (Residues: 1-499; Coverage: 100%)
Gene name: PYK1
Sequence domains:
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand MG 2 x MG
Ligand K 2 x K
Ligand AKG 2 x AKG
Ligand FDP 2 x FDP
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: I222
Unit cell:
a: 103.25Å b: 108.01Å c: 265.82Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.158 0.193
Expression system: Escherichia coli

Quick links

Citations

1 review citation

The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes: multifunctional enzymes from microbes to mitochondria.
Weiss et al. (2018)
4 other articles

1 mention without citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)